Evidence map›Paper›PMID 12376635›Full record

ArticlePlant physiology2002

The calcium-binding activity of a vacuole-associated, dehydrin-like protein is regulated by phosphorylation.

Bruce J Heyen, Muath K Alsheikh, Elizabeth A Smith, Carl F Torvik, Darren F Seals, Stephen K Randall

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
2.4field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

52 citing papers in PubMed, 151 citations in OpenAlex.

  1. Article
  2. Plants (Basel, Switzerland) · 2026
    Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Structural disorder in plant proteins: where plasticity meets sessility.Cellular and molecular life sciences : CMLS · 2017
    Review
  14. Article
  15. Article
  16. Effect ofFrontiers in plant science · 2017
    Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Bruce J HeyenDepartment of Biology, Indiana University-Purdue University at Indianapolis, 723 West Michigan Street, Indianapolis, IN 46202-5132, USA.
Muath K Alsheikh
Elizabeth A Smith
Carl F Torvik
Darren F Seals
Stephen K Randall
Indiana University – Purdue University Indianapolis · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A vacuole membrane-associated calcium-binding protein with an apparent mass of 45 kD was purified from celery (Apium graveolens). This protein, VCaB45, is enriched in highly vacuolate tissues and is located within the lumen of vacuoles. Antigenically related proteins are present in many dicotyledonous plants. VCaB45 contains significant amino acid identity with the dehydrin family signature motif, is antigenically related to dehydrins, and has a variety of biochemical properties similar to dehydrins. VCaB45 migrates anomalously in sodium dodecyl sulfate-polyacrylamide gel electrophoresis having an apparent molecular mass of 45 kD. The true mass as determined by matrix-assisted laser-desorption ionization time of flight was 16.45 kD. VCaB45 has two characteristic dissociation constants for calcium of 0.22 +/- 0.142 mM and 0.64 +/- 0.08 mM, and has an estimated 24.7 +/- 11.7 calcium-binding sites per protein. The calcium-binding properties of VCaB45 are modulated by phosphorylation; the phosphorylated protein binds up to 100-fold more calcium than the dephosphorylated protein. VCaB45 is an "in vitro" substrate of casein kinase II (a ubiquitous eukaryotic kinase), the phosphorylation resulting in a partial activation of calcium-binding activity. The vacuole localization, calcium binding, and phosphorylation of VCaB45 suggest potential functions.

Indexed as

Acid PhosphataseAlkaline PhosphataseAmino Acid SequenceApiumBlotting, WesternCalciumCalcium-Binding ProteinsElectrophoresis, Polyacrylamide GelMolecular Sequence DataPhosphorylationPhosphotransferasesPlant ProteinsSequence Homology, Amino AcidVacuolesAcid PhosphataseAlkaline PhosphataseCalciumCalcium-Binding Proteinsdehydrin-like protein, plantPhosphotransferasesPlant Proteins

Identifiers

PMID12376635
PMCPMC166597
OpenAlexW2152116676

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.